Predicting the binding properties of cibacron blue F3GA in affinity separation systems

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dc.contributor.authorAndac, Cenk A.
dc.contributor.authorAndac, Muge
dc.contributor.authorDenizli, Adil
dc.date.accessioned2024-04-24T16:14:52Z
dc.date.available2024-04-24T16:14:52Z
dc.date.issued2007
dc.departmentDicle Üniversitesien_US
dc.description.abstractThe binding properties of cibacron blue F3GA (CB-F3GA) bound to a model NAD(P)H/FAD(H-2)-dependent protein system, namely cytosolic quinone reductase (QR), was characterized by AMBER in an attempt to address the binding properties of immobilized CB-F3GA used in the separation of serum albumin. A favorable binding free energy of -4.52 kcal/mol (K-D = 5.09 x 10(-4) kcal/mol) was determined for CB-F3GA binding by MM-PBSA method, which was found to be a ballpark estimate of empirical values reported in literature (Delta G approximate to -6 kcal/mol). We propose that CB-F3GA primarily follows a class III binding motif in presence of FAD in the binding site of QR in solution, while a class II binding motif is observed in the crystal form. It was found that favorable van der Waals/hydrophobic interactions take place in the binding site making a major contribution to a favorably dominating enthalpy of binding (Delta H-tot = -25.87 kcal/mol) as compared to a disfavorable binding entropy term (T Delta S-tot = -21.35 kcal/mol). Additional MM-PBSA experiments in the absence of FAD gave rise to a disfavorable binding free energy for CB in complex with QR, suggesting that FAD is an essential determinant of CB-F3GA binding. This is in contrast to an earlier observation of Denizli et al. on separation of human serum albumin (HSA) by immobilized CB-F3GA in the absence of FAD. Therefore, a class I binding model for CB-F3GA is proposed here to account for the efficient separation of HSA in affinity chromatography systems. (C) 2007 Elsevier B.V. All rights reserved.en_US
dc.identifier.doi10.1016/j.ijbiomac.2007.06.008
dc.identifier.endpage438en_US
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.issue4en_US
dc.identifier.pmid17675148
dc.identifier.scopus2-s2.0-34548254923
dc.identifier.scopusqualityQ1
dc.identifier.startpage430en_US
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2007.06.008
dc.identifier.urihttps://hdl.handle.net/11468/15473
dc.identifier.volume41en_US
dc.identifier.wosWOS:000249845900010
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCibacron Blue F3gaen_US
dc.subjectQuinone Reductaseen_US
dc.subjectHsaen_US
dc.subjectMolecular Dynamicsen_US
dc.subjectAffinityen_US
dc.subjectAmberen_US
dc.subjectMm-Pbsaen_US
dc.subjectElectrostatic Surface Mapen_US
dc.titlePredicting the binding properties of cibacron blue F3GA in affinity separation systemsen_US
dc.titlePredicting the binding properties of cibacron blue F3GA in affinity separation systems
dc.typeArticleen_US

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